ID A0A1A5YN17_9BACL Unreviewed; 164 AA.
AC A0A1A5YN17;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 05-FEB-2025, entry version 23.
DE RecName: Full=Probable chemoreceptor glutamine deamidase CheD {ECO:0000256|HAMAP-Rule:MF_01440};
DE EC=3.5.1.44 {ECO:0000256|HAMAP-Rule:MF_01440};
GN Name=cheD {ECO:0000256|HAMAP-Rule:MF_01440};
GN ORFNames=A7K91_16315 {ECO:0000313|EMBL:OBR66800.1};
OS Paenibacillus oryzae.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Paenibacillus.
OX NCBI_TaxID=1844972 {ECO:0000313|EMBL:OBR66800.1, ECO:0000313|Proteomes:UP000092024};
RN [1] {ECO:0000313|EMBL:OBR66800.1, ECO:0000313|Proteomes:UP000092024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1DrF-4 {ECO:0000313|EMBL:OBR66800.1,
RC ECO:0000313|Proteomes:UP000092024};
RA Zhang J., Zhang X.;
RT "Paenibacillus oryzae. sp. nov., isolated from the rice root.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably deamidates glutamine residues to glutamate on
CC methyl-accepting chemotaxis receptors (MCPs), playing an important role
CC in chemotaxis. {ECO:0000256|HAMAP-Rule:MF_01440}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutaminyl-[protein] + H2O = L-glutamyl-[protein] + NH4(+);
CC Xref=Rhea:RHEA:16441, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:10208,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29973,
CC ChEBI:CHEBI:30011; EC=3.5.1.44; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01440};
CC -!- SIMILARITY: Belongs to the CheD family. {ECO:0000256|HAMAP-
CC Rule:MF_01440}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBR66800.1}.
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DR EMBL; LYPA01000043; OBR66800.1; -; Genomic_DNA.
DR RefSeq; WP_068681102.1; NZ_LYPA01000043.1.
DR AlphaFoldDB; A0A1A5YN17; -.
DR STRING; 1844972.A7K91_16315; -.
DR OrthoDB; 9807202at2; -.
DR Proteomes; UP000092024; Unassembled WGS sequence.
DR GO; GO:0050568; F:protein-glutamine glutaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR CDD; cd16352; CheD; 1.
DR Gene3D; 3.30.1330.200; -; 1.
DR HAMAP; MF_01440; CheD; 1.
DR InterPro; IPR038592; CheD-like_sf.
DR InterPro; IPR005659; Chemorcpt_Glu_NH3ase_CheD.
DR InterPro; IPR011324; Cytotoxic_necrot_fac-like_cat.
DR PANTHER; PTHR35147; CHEMORECEPTOR GLUTAMINE DEAMIDASE CHED-RELATED; 1.
DR PANTHER; PTHR35147:SF1; CHEMORECEPTOR GLUTAMINE DEAMIDASE CHED-RELATED; 1.
DR Pfam; PF03975; CheD; 1.
DR SUPFAM; SSF64438; CNF1/YfiH-like putative cysteine hydrolases; 1.
PE 3: Inferred from homology;
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|HAMAP-
KW Rule:MF_01440};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01440};
KW Reference proteome {ECO:0000313|Proteomes:UP000092024}.
SQ SEQUENCE 164 AA; 17496 MW; ECEC323768797ABA CRC64;
MTEQTLIKVG MADLNIGLAG AILKTTGLGS CVGLTLFDPV AKVAGMAHVM LPSSEIAREA
QINAAKYADT AIPLLLQRME NSGAKLLRME AKMAGGAQMF AFSGQGDSLR IGPRNVESCL
VLLQQYRIPV RSQDTGGNFG RTVEFDSISG MLLIRSMQHG VKEI
//
